Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA. Determined by X-ray diffraction at 7.5 Å resolution. Released 2 Dec 2008.
Explore 3DL8 in 3D Show helices and sheets RCSB PDB PDBe
3DL8 contains 96 α-helices and 46 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-33 | 25 | |
| α-helix | 39-51 | 13 | |
| α-helix | 59-76 | 18 | |
| α-helix | 86-94 | 9 | |
| β-strand | 97-98 | 2 | 1 |
| α-helix | 107-118 | 12 | |
| β-strand | 124-128 | 5 | 1 |
| α-helix | 131-140 | 10 | |
| α-helix | 142-147 | 6 | |
| β-strand | 154 | 1 | 1 |
| α-helix | 164-169 | 6 | |
| β-strand | 172-176 | 5 | 1 |
| α-helix | 177-186 | 10 | |
| β-strand | 204-207 | 4 | 1 |
| β-strand | 221 | 1 | 2 |
| α-helix | 230-246 | 17 | |
| α-helix | 263-271 | 9 | |
| α-helix | 284-299 | 16 | |
| β-strand | 307 | 1 | 3 |
| β-strand | 314 | 1 | 3 |
| β-strand | 316 | 1 | 4 |
| β-strand | 324 | 1 | 4 |
| α-helix | 333-341 | 9 | |
| β-strand | 352 | 1 | 2 |
| α-helix | 356-361 | 6 | |
| β-strand | 367-370 | 4 | 1 |
| α-helix | 376-380 | 5 | |
| α-helix | 381-385 | 5 | |
| β-strand | 401-408 | 8 | 5 |
| α-helix | 413-428 | 16 | |
| β-strand | 432-436 | 5 | 5 |
| α-helix | 439-452 | 14 | |
| β-strand | 457-459 | 3 | 5 |
| α-helix | 464-473 | 10 | |
| β-strand | 480-484 | 5 | 5 |
| α-helix | 499-501 | 3 | |
| β-strand | 506-509 | 4 | 5 |
| α-helix | 516-524 | 9 | |
| β-strand | 534-540 | 7 | 5 |
| α-helix | 545-548 | 4 | |
| α-helix | 551-559 | 9 | |
| β-strand | 569 | 1 | 5 |
| α-helix | 574-619 | 46 | |
| α-helix | 624-640 | 17 | |
| α-helix | 654-663 | 10 | |
| α-helix | 682-701 | 20 | |
| α-helix | 705-714 | 10 | |
| α-helix | 715-719 | 5 | |
| α-helix | 720-741 | 22 | |
| α-helix | 750-776 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-61 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-31 | 23 | |
| α-helix | 53-70 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-33 | 19 | |
| α-helix | 77-93 | 17 | |
| α-helix | 106-137 | 32 | |
| α-helix | 153-157 | 5 | |
| α-helix | 158-179 | 22 | |
| α-helix | 184-196 | 13 | |
| α-helix | 216-232 | 17 | |
| β-strand | 245 | 1 | 11 |
| β-strand | 251 | 1 | 11 |
| α-helix | 274-290 | 17 | |
| α-helix | 308-315 | 8 | |
| α-helix | 316-323 | 8 | |
| α-helix | 324-327 | 4 | |
| α-helix | 332-338 | 7 | |
| β-strand | 344 | 1 | 12 |
| β-strand | 348 | 1 | 12 |
| α-helix | 353-385 | 33 | |
| α-helix | 398-417 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein translocase subunit secA | A, B | protein | 779 | Bacillus subtilis | P28366 (AlphaFold model) |
| Preprotein translocase subunit secY | G, H | protein | 429 | Aquifex aeolicus | O66491 (AlphaFold model) |
| SecE | C, D | protein | 65 | Aquifex Aeolicus | D0VWU4 (AlphaFold model) |
| Protein-export membrane protein secG | E, F | protein | 107 | Aquifex aeolicus | O66505 (AlphaFold model) |
>3DL8_1 Protein translocase subunit secA (chains A, B) MLGILNKMFDPTKRTLNRYEKIANDIDAIRGDYENLSDDALKHKTIEFKERLEKGATTDD LLVEAFAVVREASRRVTGMFPFKVQLMGGVALHDGNIAEMKTGEGKTLTSTLPVYLNALT GKGVHVVTVNEYLASRDAEQMGKIFEFLGLTVGLNLNSMSKDEKREAYAADITYSTNNEL GFDYLRDNMVLYKEQMVQRPLHFAVIDEVDSILIDEARTPLIISGQAAKSTKLYVQANAF VRTLKAEKDYTYDIKTKAVQLTEEGMTKAEKAFGIDNLFDVKHVALNHHINQALKAHVAM QKDVDYVVEDGQVVIVDSFTGRLMKGRRYSEGLHQAIEAKEGLEIQNESMTLATITFQNY FRMYEKLAGMTGTAKTEEEEFRNIYNMQVVTIPTNRPVVRDDRPDLIYRTMEGKFKAVAE DVAQRYMTGQPVLVGTVAVETSELISKLLKNKGIPHQVLNAKNHEREAQIIEEAGQKGAV TIATNMAGRGTDIKLGEGVKELGGLAVVGTERHESRRIDNQLRGRSGRQGDPGITQFYLS MEDELMRRFGAERTMAMLDRFGMDDSTPIQSKMVSRAVESSQKRVEGNNFDSRKQLLQYD DVLRQQREVIYKQRFEVIDSENLREIVENMIKSSLERAIAAYTPREELPEEWKLDGLVDL INTTYLDEGALEKSDIFGKEPDEMLELIMDRIITKYNEKEEQFGKEQMREFEKVIVLRAV DSKWMDHIDAMDQLRQGIHLRAYAQTNPLREYQMEGFAMFEHMIESIEDEVAKFVMKAE
>3DL8_2 Preprotein translocase subunit secY (chains G, H) MSEYLKALFELKELRQKFIFTLLMFVIYRLGSHIPIPGINPEALRDFLKAFEGSVFALYD IFSGGNLGRLTVFALGVMPYISASIMMQLLTVAIPSLQRLAKEEGDYGRYKINEYTKYLT LFVATVQSLGIAFWIRGQVSPKGIPVVENPGISFILITVLTLVAGTMFLVWIADRITEKG IGNGASLIIFAGIVANFPNAVIQFYEKVKTGDIGPLTLLLIIALIIAIIVGIVYVQEAER RIPIQYPGRQVGRQLYAGRKTYLPIKINPAGVIPIIFAQALLLIPSTLLNFVQNPFIKVI ADMFQPGAIFYNFLYVTFIVFFTYFYTAVLINPVELAENLHKAGAFIPGVRPGQDTVKYL ERIINRLIFFGALFLSVIALIPILISVWFNIPFYFGGTTALIVVGVALDTFRQIETYLIQ KKYKSYVRR
>3DL8_3 SecE (chains C, D) MEKLKEFLKGVRDELKRVVWPSRELVVKATISVIIFSLAIGVYLWILDLTFTKIISFILS LRGSL
>3DL8_4 Protein-export membrane protein secG (chains E, F) MYYALLTLFVIIAVVLIISTLLQKGRGDVGAAFGGGMGQSIFGVGGVETILTKATYWLGA LFLVLALLLSVIPKEKGSVVEKSVQTEQSEGKGTTQESGKGHHHHHH
Structure of a complex of the ATPase SecA and the protein-translocation channel. Zimmer, J., Nam, Y., Rapoport, T.A. Nature (2008) 455:936-943. DOI 10.1038/nature07335 · PubMed
Other PDB entries of the same protein (UniProt P28366 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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